ArticleJournal of molecular biology2007
Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 105 citations in OpenAlex.
- Proteomic compensation by paralogs preserves protein interaction networks after gene loss in cancer.Molecular systems biology · 2025Article
- A highly conserved neuronal microexon in DAAM1 controls actin dynamics, RHOA/ROCK signaling, and memory formation.Nature communications · 2025Article
- Nucleating amoeboid cancer cell motility with Diaphanous related formins.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Genome-wide identification, characterization and expression profiles of FORMIN gene family in cotton (Gossypium Raimondii L.).BMC genomic data · 2024Article
- The dishevelled associated activator of morphogenesis protein 2 (Daam2) regulates neural tube closure.Developmental dynamics : an official publication of the American Association of Anatomists · 2024Article
- Reversion induced LIM domain protein (RIL) is a Daam1-interacting protein and regulator of the actin cytoskeleton during non-canonical Wnt signaling.Developmental biology · 2024Article
- Formin Binding Protein 1 (FNBP1) regulates non-canonical Wnt signaling and vertebrate gastrulation.Developmental biology · 2024Article
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- FRL and DAAM are required for lateral adhesion of interommatidial cells and patterning of the retinal floor.Development (Cambridge, England) · 2023Article
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- Alterations to the broad-spectrum formin inhibitor SMIFH2 modulate potency but not specificity.Scientific reports · 2022Article
- Molecular Dissection of DAAM Function during Axon Growth in Drosophila Embryonic Neurons.Cells · 2022Article
- The Actin Regulators Involved in the Function and Related Diseases of Lymphocytes.Frontiers in immunology · 2022Review
- Cooperative bundling by fascin generates actin structures with architectures that depend on filament length.Frontiers in cell and developmental biology · 2022Article
- Regional heterogeneity of astrocyte morphogenesis dictated by the formin protein, Daam2, modifies circuit function.EMBO reports · 2021Article
- The genetic architecture of structural left-right asymmetry of the human brain.Nature human behaviour · 2021Article
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- Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer.Cell proliferation · 2021Article
- EhC2B, a C2 domain-containing protein, promotes erythrophagocytosis in Entamoeba histolytica via actin nucleation.PLoS pathogens · 2020Article
- PTPN3 suppresses lung cancer cell invasiveness by counteracting Src-mediated DAAM1 activation and actin polymerization.Oncogene · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Daam1 (dishevelled-associated activator of morphogenesis-1) is a diaphanous-related formin first studied as a novel dishevelled binding protein and shown to be crucial for the planar cell polarity (PCP) pathway in Xenopus. Daam1, like other formins, directs nucleation and elongation of new actin filaments using its conserved formin-homology-2 (FH2) domain. Here we report the crystal structure of a large C-terminal fragment of human Daam1 containing the FH2 domain. The structure, determined at 2.25 A resolution using the single-wavelength anomalous diffraction (SAD) phasing method, reveals a "tethered dimer" architecture that is similar to that previously described for the FH2 domain of the yeast formin Bni1, which shares approximately 21% sequence identity with Daam1. Despite the overall similarity with the dimeric FH2 domain of Bni1 and with a truncated monomeric structure of mDia1, the Daam1 FH2 structure reveals a number of differences in secondary structure elements and in the "lasso/post" dimerization interface that may be functionally important. Most strikingly, the two halves of the crystallographic dimer pack together in a manner that occludes their actin binding surfaces. This "locked" conformation is stabilized by two novel, interacting beta-strands formed by the ends of the linkers that connect the two sides of the dimer. The Daam1 FH2 domain has weak actin assembly activity as compared with other mammalian formins, but mutations that disrupt the beta-strand lock increase activity about tenfold to a level comparable to other formins, suggesting that this occluded conformation may represent an auto-inhibited conformation of the Daam1 FH2 domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.